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APOC2 encodes a lipid-binding protein belonging to the apolipoprotein gene family. Additionally we are shipping Apolipoprotein C-II Antibodies (109) and Apolipoprotein C-II Kits (49) and many more products for this protein.
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the apoc2 mutant zebrafish is a robust and versatile animal model to study hypertriglyceridemia.
The results highlight the importance of charge-pair interactions within the apoC-II fibril core
Conformational rearrangement of apoC-II at lipoprotein surfaces promotes interaction with LPL (show LCP1 Proteins).
Large deletion in APOC2 caused by Alu-Alu homologous recombination is associated with with apolipoprotein C-II deficiency.
No APOC2 mutations were identified in a cohort of patients with diabetic lipemia.
Six apolipoproteins (APOA1 (show APOA1 Proteins), APOA2 (show APOA2 Proteins), APOB (show APOB Proteins), APOC2, APOC3 (show APOC3 Proteins), and APOE (show APOE Proteins)) were able to differentiate bladder cancer from hernia. SAA4 (show SAA4 Proteins) was significantly increased in bladder cancer subgroups, whereas ProEGF was significantly decreased in bladder cancer subgroups.
STAT1 (show STAT1 Proteins) bound on multienhancer 2 cooperates with RXRalpha (show RXRA Proteins) located on apoCII promoter and upregulates apoCII expression only in macrophages.
Mutations in GPIHBP1 (show GPIHBP1 Proteins) are rare but the associated clinical phenotype of hypertriglyceridaemia is severe
These results support a predictive change in the ratio of plasma ApoCIII (show APOC3 Proteins) to ApoCII in pregnancies complicated by severe preeclampsia.
Substoichiometric concentrations of cyc (show CYCS Proteins)[60-70] significantly delayed fibril formation by the fibrillogenic, linear peptides apoC-II[60-70] and apoC-II[56-76].
Activation of apoC-II fibrils by submicellar lipid (NBD-lyso-12-phosphocholine) is catalytic with release of monomer- and tetramer-bound lipid accompanying fibril elongation and growth.
A novel mouse model of apoC-II deficiency was created with an apoC-II peptide that reverses the hypertriglyceridemia.
Data show that apoC-II and LPL (show LPL Proteins) mRNAs correlate temporally and geographically with surfactant lipid synthesis in preparation for birth and suggest that fatty acid recruitment from the circulation by apoC-II-activated LPL (show LPL Proteins) is modulated by apoC-II secretion.
TR4 (show NR2C2 Proteins) can also regulate apolipoprotein E (show APOE Proteins), C-I, and C-II gene expression via the TR4 (show NR2C2 Proteins) response element within the hepatic control region
This gene encodes a lipid-binding protein belonging to the apolipoprotein gene family. The protein is secreted in plasma where it is a component of very low density lipoprotein. This protein activates the enzyme lipoprotein lipase, which hydrolyzes triglycerides and thus provides free fatty acids for cells. Mutations in this gene cause hyperlipoproteinemia type IB, characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis. This gene is present in a cluster with other related apolipoprotein genes on chromosome 19. Naturally occurring read-through transcription exists between this gene and the neighboring upstream apolipoprotein C-IV (APOC4) gene.
, apolipoprotein C2